Radiofrequency pulse shaping has previously been shown to give enhanced magnetic resonance images and improved suppression of the water signal in nuclear magnetic resonance spectroscopy of small molecules in solution. We propose to extend this technique to study glucagon, whose aggregation dynamics are analogous to protein folding, and to study the actin:profilin complex, which plays a central role in muscle contraction. We will modify an existing commercial high field NMR to make pulse shaping routinely available. We will also, in a collaborative effort, demonstrate improved bandwidth and reduced amplifier dead time for Fourier transform electron paramagentic resonance. Finally, we ill continue our computational efforts to develop more useful shapes, and apply a new theoretical formalism to make quantitative predictions about directions for further improvement.